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| {{STRUCTURE_1bfg| PDB=1bfg | SCENE= }} | | {{STRUCTURE_1bfg| PDB=1bfg | SCENE= }} |
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| '''CRYSTAL STRUCTURE OF BASIC FIBROBLAST GROWTH FACTOR AT 1.6 ANGSTROMS RESOLUTION'''
| | ===CRYSTAL STRUCTURE OF BASIC FIBROBLAST GROWTH FACTOR AT 1.6 ANGSTROMS RESOLUTION=== |
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| ==Overview==
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| We have determined the crystal structures of two types of human basic fibroblast growth factor, the serine analogue and the wild-type, at 1.6 and 2.5 A resolution, respectively. Two good heavy atom derivatives were found and used for multiple isomorphous replacement phasing. The atomic coordinates were refined using the Hendrickson & Konnert program for stereochemically restrained refinement against structure factors. The crystallographic R factors were reduced to 15.3% for the serine analogue structure and 16.0% for the wild-type structure. The serine analogue and wild-type structures have been found to be almost identical, the root-mean-square deviation between the corresponding C alpha atoms being 0.11 A. Their structures are composed of twelve beta-strands forming a barrel and three loops. Their molecules have an approximate threefold internal symmetry and are similar in architecture to that of interleukin-1 beta. A possible heparin-binding site, which comprises five basic residues, Lys119, Arg120, Lys125, Lys129, and Lys135, has been revealed by calculating the electrostatic potential energy.
| | The line below this paragraph, {{ABSTRACT_PUBMED_1769963}}, adds the Publication Abstract to the page |
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| | {{ABSTRACT_PUBMED_1769963}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Matsuura, Y.]] | | [[Category: Matsuura, Y.]] |
| [[Category: Growth factor]] | | [[Category: Growth factor]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 11:26:45 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 19:02:28 2008'' |